Ras-related protein Rab-32 (RAB32) is a 225-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q13637.
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The mean pLDDT of this model is 83.8 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.
| pLDDT band | Meaning | Share of residues |
|---|---|---|
| Above 90 | Very high: backbone and side chains are usually accurate | 64% |
| 70 to 90 | Confident: backbone generally right | 14% |
| 50 to 70 | Low: treat with caution | 10% |
| Below 50 | Very low: often disordered regions | 12% |
What pLDDT means and how to read it
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:11784320, PubMed:21808068). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:11784320). Also acts as an A-kinase anchoring protein by binding to the type II regulatory subunit of protein kinase A and anchoring it to the mitochondrion. Also involved in synchronization of mitochondrial fission (PubMed:12186851). Plays a role in the maturation of…
Interacts with ANKRD27 (PubMed:21269460, PubMed:24856514). A decreased interaction with ANKRD27 seen in the presence of SGSM2 (PubMed:21269460). Interacts with LRRK2 (via N-terminus); this interaction results in stimulation of RAB10 phosphorylation by LRRK2 (PubMed:38127736, PubMed:38858457)
Mitochondrion, Mitochondrion outer membrane, Cytoplasmic vesicle, phagosome, Cytoplasmic vesicle, phagosome membrane, Melanosome, Melanosome membrane
Compare the prediction with experimentally determined structures of the same protein:
| PDB ID | Method | Resolution | Chains and residues |
|---|---|---|---|
| 6FF8 | X-ray | 2.13 Å | A/B=20-198 |
| 5OEC | X-ray | 2.3 Å | B=20-201 |
| 4CYM | X-ray | 2.8 Å | A/B/C=1-225 |
| 5OED | X-ray | 2.9 Å | B=20-201 |
| 4CZ2 | X-ray | 2.97 Å | A/B/C=1-225 |
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